Faculty Opinions recommendation of Delineating the conformational landscape of the adenosine A2A receptor during G protein coupling.

2021 ◽  
Author(s):  
Andrew Goryachev
Keyword(s):  
G Protein ◽  
Adenosine A2a Receptor ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
A2a Receptor ◽  
Conformational Landscape ◽  
Adenosine A2a

Delineating the conformational landscape of the adenosine A2A receptor during G protein coupling

Cell ◽  
2021 ◽  
Author(s):  
Shuya Kate Huang ◽  
Aditya Pandey ◽  
Duy Phuoc Tran ◽  
Nicolas L. Villanueva ◽  
Akio Kitao ◽  
...  
Keyword(s):  
G Protein ◽  
Adenosine A2a Receptor ◽  
G Protein Coupling ◽  
Protein Coupling ◽  
A2a Receptor ◽  
Conformational Landscape ◽  
Adenosine A2a

scholarly journals Dynamic Role of the G Protein in Stabilizing the Active State of the Adenosine A2A Receptor

Structure ◽  
2019 ◽  
Vol 27 (4) ◽  
pp. 703-712.e3 ◽  
Author(s):  
Sangbae Lee ◽  
Anita K. Nivedha ◽  
Christopher G. Tate ◽  
Nagarajan Vaidehi
Keyword(s):  
G Protein ◽  
Adenosine A2a Receptor ◽  
Active State ◽  
A2a Receptor ◽  
Adenosine A2a

Stabilised G protein-coupled receptors in structure-based drug design: a case study with adenosine A2A receptor

MedChemComm ◽  
2013 ◽  
Vol 4 (1) ◽  
pp. 52-67 ◽  
Author(s):  
Stephen P. Andrews ◽  
Benjamin Tehan
Keyword(s):  
Parkinson’S Disease ◽  
Drug Design ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
Adenosine A2a Receptor ◽  
Structure Based Drug Design ◽  
A2a Receptor ◽  
Adenosine A2a ◽  
G Protein Coupled

The first example of structure-based drug design with stabilised GPCRs has enabled the identification of a preclinical candidate for the treatment of Parkinson's disease.

scholarly journals Structure of the adenosine A2A receptor bound to an engineered G protein

Nature ◽  
2016 ◽  
Vol 536 (7614) ◽  
pp. 104-107 ◽  
Author(s):  
Byron Carpenter ◽  
Rony Nehmé ◽  
Tony Warne ◽  
Andrew G. W. Leslie ◽  
Christopher G. Tate
Keyword(s):  
G Protein ◽  
Adenosine A2a Receptor ◽  
A2a Receptor ◽  
Adenosine A2a

scholarly journals Erratum: Structure of the adenosine A2A receptor bound to an engineered G protein

Nature ◽  
2016 ◽  
Vol 538 (7626) ◽  
pp. 542-542 ◽  
Author(s):  
Byron Carpenter ◽  
Rony Nehmé ◽  
Tony Warne ◽  
Andrew G. W. Leslie ◽  
Christopher G. Tate
Keyword(s):  
G Protein ◽  
Adenosine A2a Receptor ◽  
A2a Receptor ◽  
Adenosine A2a

scholarly journals Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Javier García-Nafría ◽  
Yang Lee ◽  
Xiaochen Bai ◽  
Byron Carpenter ◽  
Christopher G Tate
Keyword(s):  
G Protein ◽  
Binding Pocket ◽  
Adenosine A2a Receptor ◽  
Intracellular Loop ◽  
Heterotrimeric G Protein ◽  
A2a Receptor ◽  
Density Map ◽  
Adenosine A2a ◽  
G Protein Coupled ◽  
Comparable Quality

The adenosine A2A receptor (A2AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein GS. Here, we determine the structure by electron cryo-microscopy (cryo-EM) of A2AR at pH 7.5 bound to the small molecule agonist NECA and coupled to an engineered heterotrimeric G protein, which contains mini-GS, the βγ subunits and nanobody Nb35. Most regions of the complex have a resolution of ~3.8 Å or better. Comparison with the 3.4 Å resolution crystal structure shows that the receptor and mini-GS are virtually identical and that the density of the side chains and ligand are of comparable quality. However, the cryo-EM density map also indicates regions that are flexible in comparison to the crystal structures, which unexpectedly includes regions in the ligand binding pocket. In addition, an interaction between intracellular loop 1 of the receptor and the β subunit of the G protein was observed.

Sign in / Sign up

Export Citation Format

Share Document